Human T cell Cyclophilin 18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity

Journal of Molecular Biology

Volumn 277, Issue 4, 1998, Pages 763-769

  Jäschke, Anja ^a   Mi, Huaifeng ^a   Tropschug, Maximilian ^a  

^a Inst F Biochem Molekularbiologie   (Germany)

Author keywords

Aop1; Cyclophilin; Oxidative stress; Peptidyl prolyl isomerase; Protein interactions

Indexed keywords

ANTIOXIDANT; CYCLOPHILIN; CYCLOSPORIN A; DRUG BINDING PROTEIN;

ARTICLE; CIS TRANS ISOMERISM; CONTROLLED STUDY; ENZYME ACTIVITY; GENETIC CONSERVATION; HUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; T LYMPHOCYTE;

EID: 0032502895     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1644     Document Type: Article

References (49)

1. Baker E.K., Colley N.J., Zuker C.S. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13:1994;4886-4895
2. Breedon L., Nasmyth K. Regulation of the yeast HO gene. Cold Spring Habor Symp. Quant. Biol. 50:1985;643-650
3. Chae H.Z., Uhm T.B., Rhee S.G. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl Acad. Sci. USA. 91:1994;7022-7026
4. Chien C.-T., Bartel P.L., Sternglanz R., Fields S. The two-hybrid system a method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl Acad. Sci. USA. 88:1991;9578-9582
5. 2+agonists on molecular chaperones in human umbilical vein endothelial cells. Electrophoresis. 16:1995;1205-1214
6. Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340:1989;245-247
7. Fischer G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chemie Int. 33:1994;1415-1436
8. Franke E.K., Yuan H.E.H., Luban J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature. 372:1994;359-362
9. Freedman R.B., Hirst T.T., Tuit M.F. Protein disulphide isomerase building bridges in protein folding. Trends Biochem Sci. 19:1994;331-336
10. Galat A. Peptidyl-prolyl cis/trans isomerases immunophilins. Eur. J. Biochem. 216:1993;689-707
11. Gething M.-J., Sambrook J. Protein folding in the cell. Nature. 355:1992;33-45
12. Guarante L. Yeast promotors and LacZ fusions designed to study expression of cloned genes in yeast. Methods Enzmol. 101:1983;181-191
13. Haendler B., Hofer-Warbinek R., Hofer E. Complementary DNA for human T-cell cyclophilin. EMBO J. 6:1987;947-950
14. Hanes S.D., Shank P.R., Bostian K.A. Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast. 5:1989;55-72
15. Hani J., Stumpf G., Domdey H. PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases. FEBS Letters. 365:1995;198-202
16. Hartl F.-U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580
17. Hoffman C.S., Winston F. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene. 57:1987;267-272
18. Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., Sugita Y., Bannai S. Cloning and characterization of a 23 kDa stress-induced mouse peritoneal macrophage protein. J. Biol. Chem. 268:1993;18633-18636
19. Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative stress. J. Biol. Chem. 264:1989;1488-1496
20. Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E., Bayney R.M. Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. J. Biol. Chem. 268:1993;12303-12310
21. 3+, or 2-mercaptoethanol. Proc. Natl Acad. Sci. USA. 86:1989;6018-6022
22. 2 mixed-function oxidation system. J. Biol. Chem. 263:1988;4704-4711
23. Kruse M., Brunke M., Escher A., Szalay A.A., Tropschug M., Zimmermann R. Enzyme assembly after de novo synthesis in rabbit reticulocyte lysate involves molecular chaperones and immunophilins. J. Biol. Chem. 270:1995;2588-2594
24. Laemmli U.K. Cleavage of structural protein during the assembly of bacteriophage T4. Nature,. 227:1970;680-685
25. Liu J., Farmer J.D., Lane W.S., Friedman J., Weissman I., Schreiber S.L. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell. 66:1991;807-815
26. Lu K.P., Hanes S.D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547
27. Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P. Human immunodeficiency virus type 1 gag protein binds to cyclophilins A and B. Cell. 73:1993;1067-1078
28. Matouschek A., Rospert S., Schmid K., Glick B.S., Schatz G. Cyclophilin catalyzes protein folding in yeast mitochondria. Proc. Natl Acad. Sci. USA. 92:1995;6319-6323
29. Mi H., Kops O., Zimmermann E., Jäschke A., Tropschug M. A nuclear RNA-binding cyclophilin in human T-cells. FEBS Letters. 398:1996;201-205
30. Nadeau K., Das A., Walsh C.T. Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl- prolyl isomerases. J. Biol. Chem. 268:1993;1479-1487
31. Pratt W.B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268:1993;21455-21458
32. Prosperi M.T., Ferbus D., Karczinski I., Goubin G. A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins. J. Biol. Chem. 268:1993;11050-11056
33. Rassow J., Mohrs K., Koidl S., Barthelmess I.B., Pfanner N., Tropschug M. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 und Hsp60. Mol. Cell. Biol. 15:1995;2654-2662
34. Rhee S.G., Kim K.H., Chae H.Z., Yim M.B., Uchida K., Netto L.E., Stadtman E.R. Antioxidant defense mechanisms a new thiol-specific antioxidant enzyme. Ann. NY Acad. Sci. 738:1994;86-92
35. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA. 74:1977;5463-5467
36. Santoro N., Thiele D.J. Oxidative stress responses in the yeast Saccharomyces cerevisiae. Hohmann S., Mager W.H. Yeast Stress Responses. 1997;171-211 Springer, New York
37. Schmid F.-X. Prolyl isomerase enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22:1993;123-142
38. Schreiber S.L. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science. 251:1991;283-287
39. Standaert R.F., Galat A., Verdine G.L., Schreiber S.L. Molecular cloning and overexpression of the human FK506-binding protein FKBP. Nature. 346:1990;671-674
40. Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N. Alkyl hydroperoxide reductase from Salmonella typhimurium. J. Biol. Chem. 265:1990;10535-10540
41. Thali M., Bukovsky A., Kondo E., Rosenwirth B., Walsh C.T., Sodrosky J., Gottlinger H.G. Functional association of cyclophilin A with HIV-1 virions. Nature. 372:1994;363-365
42. Tropschug M. Neurospora crassa cyclophilins. Gething M.-J. Guidebook to Molecular Chaperones and Protein-Folding Catalysts. 1997;382-384 Sambrook & Tooze at Oxford University Press, Oxford
43. Tropschug M., Nicholson D.W., Hartl F.-U., Köhler H., Pfanner N., Wachter E., Neupert W. Cyclosporin A-binding protein of N. crassa one gene codes for both the cytosolic and mitochondrial forms. J. Biol. Chem. 263:1988;14433-14440
44. Tropschug M., Barthelmess I.B., Neupert W. Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae. Nature. 342:1989;953-955
45. Tsuji K., Copeland N.G., Jenkins N.A., Obinata M. Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli. Biochem J. 307:1995;377-381
46. von Ahsen O., Tropschug M., Pfanner N., Rassow J. The chaperonin-cycle cannot substitute for prolyl isomerase activity, but GroEl alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form. EMBO J. 16:1997;4568-4578
47. Yamamoto T., Matsui Y., Natori S., Obinata M. Cloning of a housekeeping-type gene (MER5) prefferentially expressed in murine erythroleukemia cells. Gene. 80:1989;337-343
48. Yang W.-M., Inouye C.J., Seto E. Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity. J. Biol. Chem. 270:1995;15187-15193
49. Yim M.B., Chae H.Z., Rhee S.G., Chock B.P., Stadtman E.R. On the protective mechanism of the thiol-specific antioxidant enzyme against the oxidative damage of biomacromolecules. J. Biol. Chem. 269:1994;1621-1626